ID   KDSB1_BURCM             Reviewed;         263 AA.
AC   Q0BCH2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            EC=2.7.7.38 {ECO:0000255|HAMAP-Rule:MF_00057};
DE   AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase 1 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CKS 1 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CMP-KDO synthase 1 {ECO:0000255|HAMAP-Rule:MF_00057};
GN   Name=kdsB1 {ECO:0000255|HAMAP-Rule:MF_00057}; OrderedLocusNames=Bamb_2595;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation
CC       into bacterial lipopolysaccharide in Gram-negative bacteria.
CC       {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-
CC         beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986,
CC         ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00057};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-
CC       octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-
CC       deoxy-D-manno-octulosonate and CTP: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00057}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00057}.
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DR   EMBL; CP000440; ABI88151.1; -; Genomic_DNA.
DR   RefSeq; WP_011657743.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BCH2; -.
DR   SMR; Q0BCH2; -.
DR   STRING; 339670.Bamb_2595; -.
DR   EnsemblBacteria; ABI88151; ABI88151; Bamb_2595.
DR   GeneID; 44693258; -.
DR   KEGG; bam:Bamb_2595; -.
DR   PATRIC; fig|339670.21.peg.2307; -.
DR   eggNOG; COG1212; Bacteria.
DR   OMA; FMATCAK; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000000662; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02517; CMP-KDO-Synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00057; KdsB; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR004528; KdsB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00466; kdsB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipopolysaccharide biosynthesis; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..263
FT                   /note="3-deoxy-manno-octulosonate cytidylyltransferase 1"
FT                   /id="PRO_0000370019"
SQ   SEQUENCE   263 AA;  28553 MW;  5FA1FC4AF1EBA660 CRC64;
     MTHPQPFIAV IPARLASTRL PNKPLADLGG KPMVVRVAER AREAGAQQVL IASDAQSVLD
     AARDHGFEAV LTRADHPSGT DRLAEVAATF GWSDDTVVVN VQGDEPLIDP VLVRDVASHL
     AAHPDCAIAT AAHPIHDAAD VFNPNVVKVA LDARNVAMYF SRAPIPWSRD AYLPHWPDVS
     AMPAPAFPVH RHIGLYAYRA RFLRTYPSLA QAPVEQAEQL EQLRAMWHGE RIAVLITEHA
     PEAGIDTPAD LARVQALFRP GSK